The α-synuclein (α-syn) amyloid fibrils are involved in various neurogenerative diseases. Solid-state NMR (ssNMR) has been showed as a powerful tool to study α-syn aggregates. Here, we report the H, C and N back-bone chemical shifts of a new α-syn polymorph obtained using proton-detected ssNMR spectroscopy under fast (95 kHz) magic-angle spinning conditions. The manual chemical shift assignments were cross-validated using FLYA algorithm. The secondary structural elements of α-syn fibrils were calculated using C chemical shift differences and TALOS software.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1007/s12104-024-10186-2 | DOI Listing |
Publication Analysis
Top Keywords
chemical shift
12
solid-state nmr
8
shift assignments
8
amyloid fibrils
8
nmr backbone
4
chemical
4
backbone chemical
4
assignments α-synuclein
4
α-synuclein amyloid
4
fibrils fast
4
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!